ID   SSB_BPPH2               Reviewed;         124 AA.
AC   Q38504; B3VMN9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000303|PubMed:2499869};
DE            Short=SSB {ECO:0000303|PubMed:10686098};
DE   AltName: Full=Gene product 5 {ECO:0000305};
DE            Short=gp5 {ECO:0000305};
DE   AltName: Full=Protein p5 {ECO:0000305};
GN   Name=5; Synonyms=5A;
OS   Bacillus phage phi29 (Bacteriophage phi-29).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX   NCBI_TaxID=10756;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6809534; DOI=10.1016/0378-1119(82)90149-4;
RA   Yoshikawa H., Ito J.;
RT   "Nucleotide sequence of the major early region of bacteriophage phi 29.";
RL   Gene 17:323-335(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-7, FUNCTION, AND DNA-BINDING.
RX   PubMed=2499869; DOI=10.1093/nar/17.10.3663;
RA   Martin G., Lazaro J.M., Mendez E., Salas M.;
RT   "Characterization of the phage phi 29 protein p5 as a single-stranded DNA
RT   binding protein. Function in phi 29 DNA-protein p3 replication.";
RL   Nucleic Acids Res. 17:3663-3672(1989).
RN   [4]
RP   CHARACTERIZATION, AND FUNCTION.
RX   PubMed=1899235; DOI=10.1016/s0021-9258(18)52215-8;
RA   Gutierrez C., Martin G., Sogo J.M., Salas M.;
RT   "Mechanism of stimulation of DNA replication by bacteriophage phi 29
RT   single-stranded DNA-binding protein p5.";
RL   J. Biol. Chem. 266:2104-2111(1991).
RN   [5]
RP   DNA-BINDING.
RX   PubMed=8196055; DOI=10.1006/jmbi.1994.1364;
RA   Soengas M.S., Esteban J.A., Salas M., Gutierrez C.;
RT   "Complex formation between phage phi 29 single-stranded DNA binding protein
RT   and DNA.";
RL   J. Mol. Biol. 239:213-226(1994).
RN   [6]
RP   CHARACTERIZATION, AND FUNCTION.
RX   PubMed=7473731; DOI=10.1006/jmbi.1995.0570;
RA   Soengas M.S., Gutierrez C., Salas M.;
RT   "Helix-destabilizing activity of phi 29 single-stranded DNA binding
RT   protein: effect on the elongation rate during strand displacement DNA
RT   replication.";
RL   J. Mol. Biol. 253:517-529(1995).
RN   [7]
RP   SUBUNIT.
RX   PubMed=10686098; DOI=10.1006/jmbi.2000.3521;
RA   Gascon I., Gutierrez C., Salas M.;
RT   "Structural and functional comparative study of the complexes formed by
RT   viral phi29, Nf and GA-1 SSB proteins with DNA.";
RL   J. Mol. Biol. 296:989-999(2000).
CC   -!- FUNCTION: Single-stranded DNA binding protein required for the
CC       elongation during viral DNA replication by strand displacement
CC       (PubMed:7473731, PubMed:1899235, PubMed:2499869, PubMed:8196055).
CC       Displaced viral DNA strands are transiently coated with the ssDNA-
CC       binding protein and therefore protected against nucleases
CC       (PubMed:7473731) (PubMed:2499869). The latter is then probably removed
CC       by the replisome that performs lagging strand synthesis or during the
CC       events that lead up to the recombination process (PubMed:7473731).
CC       Stimulates in vitro DNA replication several fold (PubMed:1899235). Has
CC       helix-destabilizing activity since it removes secondary structure from
CC       the ssDNA in replicative intermediates (PubMed:7473731).
CC       {ECO:0000269|PubMed:1899235, ECO:0000269|PubMed:2499869,
CC       ECO:0000269|PubMed:8196055, ECO:0000305|PubMed:7473731}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10686098}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus single-strand-binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; V01155; CAA24483.1; -; Genomic_DNA.
DR   EMBL; EU771092; ACE96026.1; -; Genomic_DNA.
DR   RefSeq; YP_002004532.1; NC_011048.1.
DR   BMRB; Q38504; -.
DR   GeneID; 6446522; -.
DR   KEGG; vg:6446522; -.
DR   Proteomes; UP000001207; Genome.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR   InterPro; IPR035408; Phi29_Phage_SSB.
DR   Pfam; PF17427; Phi29_Phage_SSB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA replication; DNA-binding; Early protein;
KW   Reference proteome; Viral DNA replication.
FT   CHAIN           1..124
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000106563"
SQ   SEQUENCE   124 AA;  13343 MW;  C65D5BABEC9910AD CRC64;
     MENTNIVKAT FDTETLEGQI KIFNAQTGGG QSFKNLPDGT IIEANAIAQY KQVSDTYGDA
     KEETVTTIFA ADGSLYSAIS KTVAEAASDL IDLVTRHKLE TFKVKVVQGT SSKGNVFFSL
     QLSL